2ebn

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[[Image:2ebn.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE==
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|PDB= 2ebn |SIZE=350|CAPTION= <scene name='initialview01'>2ebn</scene>, resolution 2.00&Aring;
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<StructureSection load='2ebn' size='340' side='right'caption='[[2ebn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2ebn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EBN FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannosyl-glycoprotein_endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.96 3.2.1.96] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ebn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebn OCA], [https://pdbe.org/2ebn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ebn RCSB], [https://www.ebi.ac.uk/pdbsum/2ebn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ebn ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ebn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebn OCA], [http://www.ebi.ac.uk/pdbsum/2ebn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ebn RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/EBA1_ELIME EBA1_ELIME] Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis.
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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/2ebn_consurf.spt"</scriptWhenChecked>
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Endo-beta-N-acetylglucosaminidase F1 (Endo F1) is an endoglycosidase, secreted by Flavobacterium meningosepticum, that cleaves asparagine-linked oligosaccharides after the first N-acetylglucosamine residue. The enzyme is selective for high-mannose oligosaccharide chains. The crystal structure of Endo F1 has been determined at 2.0-A resolution. The molecular fold consists of a highly irregular alpha/beta-barrel, a commonly observed motif consisting of a cyclic 8-fold repeat of beta-strand/loop/alpha-helix units with an eight-stranded parallel beta-barrel at the center. Endo F1 lacks two of the alpha-helices, those of units 5 and 6. Instead, the links after beta-strands 5 and 6 consist of a short turn followed by a section in an extended conformation that replaces the helix and a long loop at the bottom of the molecule. The absence of any excursion on top of the molecule following beta-strands 5 and 6 results in a pronounced depression in the rim of the barrel. This depression forms one end of a shallow cleft that runs across the surface of the molecule, over the core of the beta-barrel to the area between the loops of units 1 and 2. The active site residues, Asp130 and Glu132, are located at the carboxyl end of beta-strand 4 and extend into this cleft. These residues are surrounded by several tyrosine residues. The cleft area formed by loops 1 and 2 is lined with polar residues, mainly asparagines. The latter area is thought to be responsible for oligosaccharide binding and recognition while the protein moiety of the substrate would be located outside the molecule but adjacent to the area of loops 5 and 6.(ABSTRACT TRUNCATED AT 250 WORDS)
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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2EBN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBN OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ebn ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate., Van Roey P, Rao V, Plummer TH Jr, Tarentino AL, Biochemistry. 1994 Nov 29;33(47):13989-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7947807 7947807]
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</StructureSection>
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
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[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Van Roey P]]
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[[Category: Roey, P Van.]]
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[[Category: hydrolase(glucosidase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:46:36 2008''
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Current revision

CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE

PDB ID 2ebn

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